More than one fifth of the proteins encoded by the genome of Escherichia coli are destined
to the bacterial cell envelope. Over the past 20 years, the mechanisms by which envelope …

Exposure of cells to elevated levels of reactive oxygen species (ROS) damages DNA,
membrane lipids and proteins, which can potentially lead to cell death. In proteins, the sulfur …

The reactive species of oxygen and chlorine damage cellular components, potentially
leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to …

Arbuscular mycorrhizal fungi (AMF) and plant rhizosphere microbes reportedly enhance
plant tolerance to abiotic stresses and promote plant growth in contaminated soils. The co …

The respiratory pathogen Streptococcus pneumoniae has evolved efficient mechanisms to
resist oxidative stress conditions and to displace other bacteria in the nasopharynx. Here we …

The formation of disulfide bonds is critical to the folding of many extracytoplasmic proteins in
all domains of life. With the discovery in the early 1990s that disulfide bond formation is …

The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative
power and the DsbC/D system as its complement for isomerization of non-native disulfides …

Protein folding homeostasis in the endoplasmic reticulum (ER) requires efficient protein thiol
oxidation, but also relies on a parallel reductive process to edit disulfides during the …

The nucleotide second messenger c‐di‐GMP nearly ubiquitously promotes bacterial biofilm
formation, with enzymes that synthesize and degrade c‐di‐GMP being controlled by diverse …

Disulfide Bonds in Protein Folding and Stability | Oxidative Folding of Proteins: Basic
Principles, Cellular Regulation and Engineering | Books Gateway | Royal Society of Chemistry …